Metabolic remodeling in frataxin-deficient yeast is mediated by Cth2 and Adr1.
Identifieur interne : 000742 ( Main/Exploration ); précédent : 000741; suivant : 000743Metabolic remodeling in frataxin-deficient yeast is mediated by Cth2 and Adr1.
Auteurs : Armando Moreno-Cerme O [Espagne] ; David Alsina [Espagne] ; Elisa Cabiscol [Espagne] ; Jordi Tamarit [Espagne] ; Joaquim Ros [Espagne]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2013.
Descripteurs français
- KwdFr :
- Aconitate hydratase (métabolisme), Alcohol dehydrogenase (métabolisme), Doxycycline (pharmacologie), Facteurs de transcription (métabolisme), Glutarédoxines (métabolisme), Gènes fongiques (génétique), Modèles biologiques (MeSH), Noyau de la cellule (effets des médicaments et des substances chimiques), Noyau de la cellule (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de liaison au fer (métabolisme), Protéines de liaison à l'ADN (métabolisme), Protéines à fluorescence verte (métabolisme), Protéome (métabolisme), Protéomique (MeSH), Reproductibilité des résultats (MeSH), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (métabolisme), Stress oxydatif (effets des médicaments et des substances chimiques), Séquençage par oligonucléotides en batterie (MeSH), Transport des protéines (effets des médicaments et des substances chimiques), Tristétraproline (métabolisme).
- MESH :
- croissance et développement : Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Noyau de la cellule, Régulation de l'expression des gènes fongiques, Saccharomyces cerevisiae, Stress oxydatif, Transport des protéines.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Gènes fongiques.
- métabolisme : Aconitate hydratase, Alcohol dehydrogenase, Facteurs de transcription, Glutarédoxines, Noyau de la cellule, Protéines de Saccharomyces cerevisiae, Protéines de liaison au fer, Protéines de liaison à l'ADN, Protéines à fluorescence verte, Protéome, Saccharomyces cerevisiae, Tristétraproline.
- pharmacologie : Doxycycline.
- Modèles biologiques, Protéomique, Reproductibilité des résultats, Séquençage par oligonucléotides en batterie.
English descriptors
- KwdEn :
- Aconitate Hydratase (metabolism), Alcohol Dehydrogenase (metabolism), Cell Nucleus (drug effects), Cell Nucleus (metabolism), DNA-Binding Proteins (metabolism), Doxycycline (pharmacology), Gene Expression Regulation, Fungal (drug effects), Genes, Fungal (genetics), Glutaredoxins (metabolism), Green Fluorescent Proteins (metabolism), Iron-Binding Proteins (metabolism), Models, Biological (MeSH), Oligonucleotide Array Sequence Analysis (MeSH), Oxidative Stress (drug effects), Protein Transport (drug effects), Proteome (metabolism), Proteomics (MeSH), Reproducibility of Results (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Transcription Factors (metabolism), Tristetraprolin (metabolism).
- MESH :
- chemical , metabolism : Aconitate Hydratase, Alcohol Dehydrogenase, DNA-Binding Proteins, Glutaredoxins, Green Fluorescent Proteins, Iron-Binding Proteins, Proteome, Saccharomyces cerevisiae Proteins, Transcription Factors, Tristetraprolin.
- drug effects : Cell Nucleus, Gene Expression Regulation, Fungal, Oxidative Stress, Protein Transport, Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Genes, Fungal.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Cell Nucleus, Saccharomyces cerevisiae.
- chemical , pharmacology : Doxycycline.
- Models, Biological, Oligonucleotide Array Sequence Analysis, Proteomics, Reproducibility of Results.
Abstract
Frataxin is a mitochondrial protein involved in iron metabolism whose deficiency in humans causes Friedreich ataxia. We performed transcriptomic and proteomic analyses of conditional Yeast Frataxin Homologue (Yfh1) mutants (tetO7-YFH1) to investigate metabolic remodeling upon Yfh1 depletion. These studies revealed that Yfh1 depletion leads to downregulation of many glucose-repressed genes. Most of them were Adr1 targets, a key transcription factor required for growth in non-fermentable carbon sources. Using a GFP-tagged Adr1, we observed that Yfh1 depletion promotes the export of Adr1 from the nucleus to the cytosol without affecting its protein levels. This effect was also observed upon H2O2 treatment, but not by iron overload/starvation, indicating the presence of a regulatory pathway involved in Adr1 export and inactivation upon stress conditions. We also observed that CTH2, a gene involved in the mRNA degradation of several iron-containing enzymes, was induced upon Yfh1 depletion. Accordingly, decreased levels of aconitase and succinate dehydrogenase were observed. Nevertheless, their levels were maintained in a Δcth2 mutant even in the absence of Yfh1. From these results we can conclude that, in addition to altering iron homeostasis, frataxin depletion involves drastic metabolic remodeling governed by Adr1 and Cth2 that finally leads to downregulation of iron-sulfur proteins and other proteins involved in respiratory metabolism.
DOI: 10.1016/j.bbamcr.2013.09.019
PubMed: 24100161
Affiliations:
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(métabolisme)</term><term>Gènes fongiques (génétique)</term><term>Modèles biologiques (MeSH)</term><term>Noyau de la cellule (effets des médicaments et des substances chimiques)</term><term>Noyau de la cellule (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines de liaison au fer (métabolisme)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Protéines à fluorescence verte (métabolisme)</term><term>Protéome (métabolisme)</term><term>Protéomique (MeSH)</term><term>Reproductibilité des résultats (MeSH)</term><term>Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (croissance et développement)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Stress oxydatif (effets des médicaments et des 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cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aconitate hydratase</term><term>Alcohol dehydrogenase</term><term>Facteurs de transcription</term><term>Glutarédoxines</term><term>Noyau de la cellule</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de liaison au fer</term><term>Protéines de liaison à l'ADN</term><term>Protéines à fluorescence verte</term><term>Protéome</term><term>Saccharomyces cerevisiae</term><term>Tristétraproline</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Doxycycline</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Doxycycline</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Biological</term><term>Oligonucleotide Array Sequence Analysis</term><term>Proteomics</term><term>Reproducibility of Results</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Modèles biologiques</term><term>Protéomique</term><term>Reproductibilité des résultats</term><term>Séquençage par oligonucléotides en batterie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Frataxin is a mitochondrial protein involved in iron metabolism whose deficiency in humans causes Friedreich ataxia. We performed transcriptomic and proteomic analyses of conditional Yeast Frataxin Homologue (Yfh1) mutants (tetO7-YFH1) to investigate metabolic remodeling upon Yfh1 depletion. These studies revealed that Yfh1 depletion leads to downregulation of many glucose-repressed genes. Most of them were Adr1 targets, a key transcription factor required for growth in non-fermentable carbon sources. Using a GFP-tagged Adr1, we observed that Yfh1 depletion promotes the export of Adr1 from the nucleus to the cytosol without affecting its protein levels. This effect was also observed upon H2O2 treatment, but not by iron overload/starvation, indicating the presence of a regulatory pathway involved in Adr1 export and inactivation upon stress conditions. We also observed that CTH2, a gene involved in the mRNA degradation of several iron-containing enzymes, was induced upon Yfh1 depletion. Accordingly, decreased levels of aconitase and succinate dehydrogenase were observed. Nevertheless, their levels were maintained in a Δcth2 mutant even in the absence of Yfh1. From these results we can conclude that, in addition to altering iron homeostasis, frataxin depletion involves drastic metabolic remodeling governed by Adr1 and Cth2 that finally leads to downregulation of iron-sulfur proteins and other proteins involved in respiratory metabolism. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24100161</PMID><DateCompleted><Year>2014</Year><Month>02</Month><Day>24</Day></DateCompleted><DateRevised><Year>2017</Year><Month>09</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1833</Volume><Issue>12</Issue><PubDate><Year>2013</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Metabolic remodeling in frataxin-deficient yeast is mediated by Cth2 and Adr1.</ArticleTitle><Pagination><MedlinePgn>3326-3337</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0167-4889(13)00341-8</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamcr.2013.09.019</ELocationID><Abstract><AbstractText>Frataxin is a mitochondrial protein involved in iron metabolism whose deficiency in humans causes Friedreich ataxia. We performed transcriptomic and proteomic analyses of conditional Yeast Frataxin Homologue (Yfh1) mutants (tetO7-YFH1) to investigate metabolic remodeling upon Yfh1 depletion. These studies revealed that Yfh1 depletion leads to downregulation of many glucose-repressed genes. Most of them were Adr1 targets, a key transcription factor required for growth in non-fermentable carbon sources. Using a GFP-tagged Adr1, we observed that Yfh1 depletion promotes the export of Adr1 from the nucleus to the cytosol without affecting its protein levels. This effect was also observed upon H2O2 treatment, but not by iron overload/starvation, indicating the presence of a regulatory pathway involved in Adr1 export and inactivation upon stress conditions. We also observed that CTH2, a gene involved in the mRNA degradation of several iron-containing enzymes, was induced upon Yfh1 depletion. Accordingly, decreased levels of aconitase and succinate dehydrogenase were observed. Nevertheless, their levels were maintained in a Δcth2 mutant even in the absence of Yfh1. From these results we can conclude that, in addition to altering iron homeostasis, frataxin depletion involves drastic metabolic remodeling governed by Adr1 and Cth2 that finally leads to downregulation of iron-sulfur proteins and other proteins involved in respiratory metabolism. </AbstractText><CopyrightInformation>© 2013 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Moreno-Cermeño</LastName><ForeName>Armando</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, IRB-Lleida, Universitat de Lleida, Lleida, Spain. Electronic address: ajmoreno@unav.es.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Alsina</LastName><ForeName>David</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, IRB-Lleida, Universitat de Lleida, Lleida, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cabiscol</LastName><ForeName>Elisa</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, IRB-Lleida, Universitat de Lleida, Lleida, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tamarit</LastName><ForeName>Jordi</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, IRB-Lleida, Universitat de Lleida, Lleida, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ros</LastName><ForeName>Joaquim</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, IRB-Lleida, Universitat de Lleida, Lleida, Spain. Electronic address: joaquim.ros@cmb.udl.cat.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>10</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C074682">ADR1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C528773">Grx5 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D033862">Iron-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020543">Proteome</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C091790">TIS11 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051816">Tristetraprolin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C098527">frataxin</NameOfSubstance></Chemical><Chemical><RegistryNumber>147336-22-9</RegistryNumber><NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.1</RegistryNumber><NameOfSubstance UI="D000426">Alcohol Dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D000154">Aconitate Hydratase</NameOfSubstance></Chemical><Chemical><RegistryNumber>N12000U13O</RegistryNumber><NameOfSubstance UI="D004318">Doxycycline</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000154" MajorTopicYN="N">Aconitate Hydratase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000426" MajorTopicYN="N">Alcohol Dehydrogenase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004318" MajorTopicYN="N">Doxycycline</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005800" MajorTopicYN="N">Genes, Fungal</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D049452" MajorTopicYN="N">Green Fluorescent Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D033862" MajorTopicYN="N">Iron-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020411" MajorTopicYN="N">Oligonucleotide Array Sequence Analysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020543" MajorTopicYN="N">Proteome</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015203" MajorTopicYN="N">Reproducibility of Results</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051816" MajorTopicYN="N">Tristetraprolin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Friedreich ataxia</Keyword><Keyword MajorTopicYN="N">Iron</Keyword><Keyword MajorTopicYN="N">Oxidative stress</Keyword><Keyword MajorTopicYN="N">Yeast frataxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>05</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>09</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>09</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>10</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>10</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>2</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24100161</ArticleId><ArticleId IdType="pii">S0167-4889(13)00341-8</ArticleId><ArticleId IdType="doi">10.1016/j.bbamcr.2013.09.019</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country></list><tree><country name="Espagne"><noRegion><name sortKey="Moreno Cerme O, Armando" sort="Moreno Cerme O, Armando" uniqKey="Moreno Cerme O A" first="Armando" last="Moreno-Cerme O">Armando Moreno-Cerme O</name></noRegion><name sortKey="Alsina, David" sort="Alsina, David" uniqKey="Alsina D" first="David" last="Alsina">David Alsina</name><name sortKey="Cabiscol, Elisa" sort="Cabiscol, Elisa" uniqKey="Cabiscol E" first="Elisa" last="Cabiscol">Elisa Cabiscol</name><name sortKey="Ros, Joaquim" sort="Ros, Joaquim" uniqKey="Ros J" first="Joaquim" last="Ros">Joaquim Ros</name><name sortKey="Tamarit, Jordi" sort="Tamarit, Jordi" uniqKey="Tamarit J" first="Jordi" last="Tamarit">Jordi Tamarit</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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